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Reviewed, UniProtKB/Swiss-Prot O74634 (SYMM_CANAL)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methionyl-tRNA synthetase, mitochondrial
    EC=6.1.1.10
Alternative name(s):
    Methionine--tRNA ligase
      Short name=MetRS
Gene names
Name: MSM1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Methionyl-tRNA synthetase, mitochondrial
PRO_0000139270

Regions

Motif25 – 3713"HIGH" region
Motif329 – 3335"KMSKS" region

Sites

Binding site3321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O74634-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 129413ACD5B14728

FASTA57767,120
        10         20         30         40         50         60 
MRFKIRGPLI QLRYKSTKAF YITTPIFYVN AAPHIGHLYS MLIADTRNKW EKLNPSKESF 

        70         80         90        100        110        120 
MLTGTDEHGL KIQSTAEKLG LEPKVLVDKV SQNFSKLAEQ FDVNYDRFIR TTDNDHIELV 

       130        140        150        160        170        180 
RYFWNLMMEK GFIYTDTHSG WYSISDETFF PETQIEEVVK NGKAVKISSE TKNEVVYQEE 

       190        200        210        220        230        240 
TNYFFKLSMF QEQLIQFLKQ NPEFIKPKHR YQFILKELED TKLPDLSISR PSSRLKWSIE 

       250        260        270        280        290        300 
VPNDSTQKIY VWFDALLNYL TATKFPHGFE VQDSKFVTPE NSIWPATHVI GKDIIRFHCI 

       310        320        330        340        350        360 
YWPIFLMAAG IELPKQVIVH SHWLCDGFKM SKSLGNLVDP MEISEYYGVD PVRFFLVENS 

       370        380        390        400        410        420 
NIDDDCKFSE ELLQRSRDAV LGKYCNLISR IGGKNFSIEE AVKSFASGEF NNIREIIETY 

       430        440        450        460        470        480 
TINKDSVEGL LSSLNKLTTD LNDLYNQMDH YFTNFDYIRA IQCWWSVINQ ANQIFQSAEP 

       490        500        510        520        530        540 
WTYVKLINSP ETPAELKEKY RILNNYFVYL CAETTRISSI LIQPVMPQLS KKILDRLNVS 

       550        560        570 
GRTSEFTTLS ADLQYGSGAN SKSHKVPLEK IAPRDIK 

« Hide

References

[1]"Cloning and characterization of mitochondrial methionyl-tRNA synthetase from a pathogenic fungi Candida albicans."
Lee S.W., Jo Y.J., Kim S.
Gene 215:311-318(1998) [PubMed: 9714830] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AB006140 Genomic DNA. Translation: BAA33373.1.

3D structure databases

HSSPHSSP built from PDB template 1A8H based on UniProtKB P23395.
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.1.1.10. 1124.

Family and domain databases

InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR002304. Met-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYMM_CANAL
AccessionPrimary (citable) accession number: O74634
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents